The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
Requirement of Serine Phosphorylation for Formation of STAT-Promoter Complexes
Abstract
Members of the interleukin-6 family of cytokines bind to and activate receptors that contain a common subunit, gp130. This leads to the activation of Stat3 and Stat1, two cytoplasmic signal transducers and activators of transcription (STATs), by tyrosine phosphorylation. Serine phosphorylation of Stat3 was constitutive and was enhanced by signaling through gp130. In cells of lymphoid and neuronal origins, inhibition of serine phosphorylation prevented the formation of complexes of DNA with Stat3-Stat3 but not with Stat3-Stat1 or Stat1-Stat1 dimers. In vitro serine dephosphorylation of Stat3 also inhibited DNA binding of Stat3-Stat3. The requirement of serine phosphorylation for Stat3- Stat3⋅DNA complex formation was inversely correlated with the affinity of Stat3-Stat3 for the binding site. Thus, serine phosphorylation appears to enhance or to be required for the formation of stable Stat3-Stat3⋅DNA complexes.
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Self-citationEffects of the tumour promoter okadaic acid on intracellular protein phosphorylation and metabolism
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Cited by
Interferon-γ: an overview of signals, mechanisms and functions
Schroder, K., Hertzog, P. J., Ravasi, T., & Hume, D. A. (2004) · Journal of Leukocyte Biology · doi:10.1189/jlb.0603252 · Cited by 4,120
Interleukin-6-type cytokine signalling through the gp130/Jak/STAT pathway
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The IL-4 receptor: signaling mechanisms and biologic functions
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Metadata
- Authors
- Zhang, X., Blenis, J., Li, H.-C., Schindler, C., & Chen-Kiang, S.
- Venue
- Science
- Published
- 1995-03-31
- Volume
- 267
- Issue
- 5206
- Pages
- 1990-1994
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1984486504
- Cited by
- 573
- References
- 29
- FWCI
- 29.46
- Type
- journal article
- Language
- en
- Open access
- closed
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- Zhang, X., Blenis, J., Li, H.-C., Schindler, C., & Chen-Kiang, S. (1995). Requirement of Serine Phosphorylation for Formation of STAT-Promoter Complexes. Science. https://doi.org/10.1126/science.7701321
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